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Role of Hyphal Formation in Interactions of Candida albicans with Endothelial Cells
Open accessAbstract
The ability to change from yeast to hyphal morphology is a major virulence determinant of Candida albicans . Mutants with defined defects in filamentation regulatory pathways have reduced virulence in mice. However, is it poorly understood why hyphal formation is critical for C. albicans to cause hematogenously disseminated infections. We used recently constructed mutants to examine the role of hyphal formation in the interactions of C. albicans with endothelial cells in vitro. These interactions included the ability of the mutants to invade and injure endothelial cells. Because the formation of hyphae may influence the host inflammatory response to C. albicans , we also investigated the capacity of these mutants to stimulate endothelial cells to express E-selectin and intercellular adhesion molecule 1. We infected endothelial cells with C. albicans strains containing homozygous null mutations in the following filamentation regulatory genes: CLA4 , CPH1 , EFG1 , and TUP1 . Whereas the wild-type strain formed true hyphae on endothelial cells, we found that neither the Δ efg1 nor the Δ cph1 Δefg1 double mutant germinated. The Δ tup1 mutant formed only pseudohyphae. We also found that the Δ efg1 , Δ cph1 Δefg1 , and Δ tup1 mutants had significantly reduced capacities to invade and injure endothelial cells. Therefore, Efg1p and Tup1p contribute to virulence by regulating hyphal formation and the factors that enable C. albicans to invade and injure endothelial cells. With the exception of the Δcph1 Δefg1 mutant, all other mutants stimulated endothelial cells to express at least one of the leukocyte adhesion molecules. Therefore, the combined activities of Cph1p and Efg1p are required for C. albicans to stimulate a proinflammatory response in endothelial cells.
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“Host cell invasion and damage are likely critical virulence attributes of C. albicans because mutants with defects in these processes in vitro are highly likely to have attenuated virulence in experimental animal models of hematogenously disseminated or oropharyngeal candidiasis [5][6][7][8].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [7]
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“Furthermore, studies with killed organisms indicate that induction of endocytosis is passive on the part of the organism because killed hyphae are endocytosed as avidly as are live hyphae [5,7].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [7]
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“We have found previously that C. albicans mutants with defects in the signal transduction pathways that govern hyphal formation have a significantly reduced capacity to invade both endothelial and oral epithelial cells in vitro [5][6][7].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [7]
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“Previously, we have found that C. albicans invades both endothelial cells and oral epithelial cells in vitro by inducing its own endocytosis [4,5,7].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [7]
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Fungal pathogenicity and morphological switches
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Interactions of Fungi with Endothelial Cells
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“Other multiple mutants of C. albicans have been identified that have reduced capacity to injure endothelial cells (Davis et al., 2000; Phan et al., 2000; Bensen et al., 2002; Blankenship et al., 2003; Sanchez et al., 2004).”
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Erythrozyten als Drug Carrier für schwerlösliche Substanzen am Beispiel von Amphotericin B
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“However, when the yeast cells did not show sprouting, the culture was reported as yeast other than Candida albicans [20].”
BackgroundPulver, R. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
Aldahash, R. (2018) · Lincoln (University of Nebraska)
Role of Rim101p in the pH response in Candida albicans
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Insilico Analysis of pathogenic genes as a major rescue of Candida albicansPreprint
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Characterization of the nuclear RNase P of Candida glabrata and improvement of genome editing tools
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“This is particularly the case for C. albicans, which hyphae formation is necessary for its escape from phagocytes and for the passage through epithelia (Phan et al. 2000).”
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Metadata
- Authors
- Phan, Q. T., Belanger, P. H., & Filler, S. G.
- Affiliations
- University of California, Los Angeles (US)
- ORCID
- Filler, Scott G.
- Venue
- Infection and Immunity
- Publisher
- American Society for Microbiology
- Published
- 2000-06
- Volume
- 68
- Issue
- 6
- Pages
- 3485-3490
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC97632
- OpenAlex
- W2134152581
- Cited by
- 181
- References
- 31
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 6 · 2019: 2 · 2018: 8 · 2017: 4 · 2016: 4 · 2015: 6 · 2014: 13 · 2013: 7 · 2012: 7
- FWCI
- 6.28
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Infection and Immunity (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (P01 AI-37194, R29AI040636, R01AI019990, R01-AI19990, P01AI037194)
- National Center for Research Resources (M01RR000425)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Fungal Infections and Studies
- Keywords
- Candida albicans, hyphal development, filamentation, endothelial cells, pseudohyphae, endothelial cell invasion, leukocyte adhesion molecules, E-selectin, ICAM-1, inflammation, virulence, yeast-to-hypha transition
- MeSH terms
- Candida albicans, DNA-Binding Proteins, Endocytosis, Endothelium, Vascular, Fungal Proteins, Genes, Fungal, Humans, Morphogenesis, Mutation, Nuclear Proteins, Repressor Proteins, Transcription Factors, Protein Serine-Threonine Kinases, Intercellular Adhesion Molecule-1, E-Selectin, Saccharomyces cerevisiae Proteins
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